Related ArticlesNMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
J Biol Chem. 1999 May 14;274(20):14130-6
Authors: Huang W, Dolmer K, Gettins PG
The low density lipoprotein receptor-related protein is a member of the low density lipoprotein receptor family and contains clusters of cysteine-rich complement-like repeats of about 42 residues that are present in all members of this family of receptors. These clusters are thought to be the principal binding sites for protein ligands. We have expressed one complement-like repeat, CR8, from the cluster in lipoprotein receptor-related protein that binds certain proteinase inhibitor-proteinase complexes and used three-dimensional NMR on the 13C/15N-labeled protein to determine the structure in solution of the calcium-bound form. The structure is very similar in overall fold to repeat 5 from the low density lipoprotein receptor (LB5), with backbone root mean square deviation of 1.5 A. The calcium-binding site also appears to be homologous, with four carboxyl and two backbone carbonyl ligands. However, differences in primary structure are such that equivalent surfaces that might represent the binding interfaces are very different from one another, indicating that different domains will have very different ligand specificities.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
nmrlearner
Journal club
0
12-15-2010 12:03 PM
[NMR paper] NMR studies of lipoprotein structure.
NMR studies of lipoprotein structure.
Related Articles NMR studies of lipoprotein structure.
Annu Rev Biophys Biomol Struct. 2002;31:177-206
Authors: Cushley RJ, Okon M
Early NMR structural studies of serum lipoproteins were based on (1)H, (13)C, (31)P, and (2)H studies of lipid components. From the early studies information on composition, lipid chain dynamics and order parameters, and monolayer organization resulted. More recently, selective or complete isotopic labeling techniques, combined with multidimensional NMR spectroscopy, have...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] NMR solution structure of complement-like repeat CR3 from the low density lipoprotein
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Feb 4;275(5):3264-9
Authors: Dolmer K, Huang W, Gettins PG
We have used NMR methods to determine the...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] NMR studies of a viral protein that mimics the regulators of complement activation.
NMR studies of a viral protein that mimics the regulators of complement activation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of a viral protein that mimics the regulators of complement activation.
J Mol Biol. 1997 Sep 19;272(2):253-65
Authors: Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN
Vaccinia virus complement control protein (VCP) is a 243-residue protein that is similar in sequence to the regulators of complement activation; its...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Biochemistry. 1996 Jan 23;35(3):698-703
Authors: Butcher DJ, Nedved ML, Neiss TG, Moe GR
The structure of a 22 amino acid peptide, TPPI , that is similar to the proline repeat segment of the replication arrest protein, Tus, has been determined by 1H NMR in 50% trifluroethanol. The...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Related Articles Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Biochemistry. 1991 Jan 29;30(4):997-1004
Authors: Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID
The complement control protein (CCP) module (also known as the short consensus repeat) is a consensus sequence of about 60 amino acid residues which is thought to fold independently. It occurs over 140 times in more than 20 extracellular...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the
Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
Related Articles Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
Biochem Cell Biol. 1990 Jan;68(1):189-98
Authors: Chana RS, Treleaven WD, Parmar YI, Cushley RJ
The order of phosphatidylcholine (PC) acyl chains in the surface monolayer of very low density lipoproteins (VLDL) and low density lipoproteins (LDL) has been...
nmrlearner
Journal club
0
08-21-2010 10:48 PM
[NMR paper] NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
Related Articles NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
Free Radic Res Commun. 1990;8(3):175-83
Authors: Barenghi L, Bradamante S, Giudici GA, Vergani C
Human plasma low density lipoprotein has been oxidized at different stages in vitro and analysed by 1H, 13C, and 31P NMR spectroscopy and by biochemical methods. Information was obtained on: a) structure mobilities of lipids and on lipid-protein interactions; b) conjugated and oxo-dienes; c)...
NMR solution structure of complement-like repeat CR8 from the low density lipoprotein
Linear Mode
